PTER_DROYA
ID PTER_DROYA Reviewed; 350 AA.
AC B4PUM2;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Phosphotriesterase-related protein;
DE EC=3.1.-.-;
DE AltName: Full=Parathion hydrolase-related protein;
GN ORFNames=GE25944;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P45548};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000250|UniProtKB:P45548};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.
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DR EMBL; CM000160; EDW96639.1; -; Genomic_DNA.
DR RefSeq; XP_002096927.1; XM_002096891.2.
DR AlphaFoldDB; B4PUM2; -.
DR SMR; B4PUM2; -.
DR STRING; 7245.FBpp0270954; -.
DR EnsemblMetazoa; FBtr0272462; FBpp0270954; FBgn0242991.
DR GeneID; 6536345; -.
DR KEGG; dya:Dyak_GE25944; -.
DR eggNOG; ENOG502QQQR; Eukaryota.
DR HOGENOM; CLU_054760_0_1_1; -.
DR OMA; MVKCGFI; -.
DR OrthoDB; 972282at2759; -.
DR PhylomeDB; B4PUM2; -.
DR Proteomes; UP000002282; Chromosome 3R.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009056; P:catabolic process; IEA:InterPro.
DR CDD; cd00530; PTE; 1.
DR InterPro; IPR017947; AryldialkylPase_Zn-BS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001559; Phosphotriesterase.
DR PANTHER; PTHR10819; PTHR10819; 1.
DR Pfam; PF02126; PTE; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS01322; PHOSPHOTRIESTERASE_1; 1.
DR PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding.
FT CHAIN 1..350
FT /note="Phosphotriesterase-related protein"
FT /id="PRO_0000388682"
FT BINDING 22
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P45548"
FT BINDING 24
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P45548"
FT BINDING 169
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P45548"
FT BINDING 169
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P45548"
FT BINDING 201
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P45548"
FT BINDING 230
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P45548"
FT BINDING 298
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P45548"
SQ SEQUENCE 350 AA; 39402 MW; 2F5A903C43281701 CRC64;
MSTVQTVLGT ITPNLLGRTL THEHVALDFE HFYRPPPPDF ESELKAKISM STLGYVRLYP
YSSKENVRFY DEEALEAAKK DVLLYKKHGG GSIVENSSYG LKRNLEFIVE LAKSTGVHFI
AGTGHYIHAM QDASHASLTV EQMSDLYSKD IITGQQVNGQ MVKCGFIGEV ASVYPIHDFE
KNAIKAAGEI QEVLGCGVSM HPHRVTKAPF EIMRLYLEAG GRADKCVMSH LDRTIFDIDE
LLEFAKLGCY IQYDLFGTEC SFYQLNTSVD MISDGQRIDN LIKLIKEGLV DKLLMSHDIH
TKHRLTSYGG HGYHHIHTNI LPRMFDRGVT LEQVEQMTVT NPANWLAFDP
